Evidence and sources

Measurements

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Big picture numbers

Structures

• 8WO5
  Salmonella motor-hook complex, CCW

  Intact motor from C-ring to hook in one model: the backbone of the composite scene. Stators are not included; add them from 6YKM/8UCS. Electron microscopy, 7.4 Å.
• 8WOE
  Salmonella motor-hook complex, CW (CheY bound)

  Same motor in the clockwise state with 34 CheY bound to the C-ring; pair with 8WO5 to show the switch. Electron microscopy, 4.3 Å.
• 9N4Z
  C-ring + MS-ring, CCW (3.0 Å)

  Highest-resolution full 34-mer C-ring; best part for close-up views of the switch. Electron microscopy, 3 Å.
• 8UOX
  C-ring, CCW-locked

  CCW end of the switch morph (same chain names as 8UPL). Electron microscopy, 4.6 Å.
• 8UPL
  C-ring, CW-locked

  CW end of the switch morph (same chain names as 8UOX). FliG is 3 residues shorter in this construct. Electron microscopy, 5.4 Å.
• 8VKQ
  C-ring, CW (Singh et al.)

  Second CW C-ring model; chain names match 9N4Z (CCW), so it also works as a morph pair. Electron microscopy, 4.6 Å.
• 6SCN
  MS-ring, FliF 33-mer

  Isolated MS-ring; shows the symmetry mismatch between its rings. Electron microscopy, 3.1 Å.
• 7NVG
  Intact basal body (MS-ring to LP-ring)

  Complete basal body with export gate, rod, LP-ring and FlgD cap; high-resolution alternative to the 8WO5 core. Electron microscopy, 3.7 Å.
• 7BIN
  Export gate + rod

  Export gate FliP5Q4R1 capped by the rod (FliE, FlgB, FlgC, FlgF, FlgG). Electron microscopy, 3.2 Å.
• 7BGL
  LP-ring (bushing), 26-mer

  2.2 Å bushing through which the rod turns; includes the lipoprotein YecR and lipid A. Electron microscopy, 2.2 Å.
• 7CGB
  Hook (FlgE)

  Universal joint between rod and filament. Electron microscopy, 3.4 Å.
• 9GO6
  Hook-filament junction

  FlgE hook, FlgK and FlgL junction rings and the first flagellin layers. Electron microscopy, 2.9 Å.
• 1UCU
  Flagellin FliC, R-type filament subunit

  Classic complete atomic model of one flagellin in the straight filament; tile it with helical symmetry to build a filament. Electron microscopy, 4 Å.
• 8CXM
  E. coli filament segment (supercoiled, normal waveform)

  Ready-made multi-subunit filament piece (55 flagellins) in the normal swimming waveform. Electron microscopy, 3.21 Å.
• 6YKM
  Stator MotA5B2, Campylobacter jejuni

  H+-driven stator unit: a MotA pentamer around a MotB dimer. Plugged (inactive) form. Electron microscopy, 3.1 Å.
• 6YKP
  Stator MotA5B2, unplugged

  Plug deleted; activated form of the same stator. Electron microscopy, 2.98 Å.
• 6YSL
  Stator MotA5B2, Bacillus subtilis

  Stator from a Gram-positive bacterium; same 5:2 architecture. Electron microscopy, 3.5 Å.
• 8UCS
  Stator bound to FliG torque helices

  Shows how MotA grips the FliG C-terminal domain: the stator-rotor gear contact. Electron microscopy, 2.4 Å.
• 8ZYV
  Na+ stator PomA5PomB2, Vibrio alginolyticus

  Na+-driven stator from a polar, high-speed Vibrio motor. Electron microscopy, 3.12 Å.
• 8BRD
  Na+ stator PomA5 + PomB TM helices

  2.5 Å view of the Na+ sites in the Vibrio stator. Electron microscopy, 2.48 Å.
• 6F2D
  Export gate FliP5Q4R1

  Core of the flagellar type III export gate. Electron microscopy, 4.2 Å.
• 6S3L
  Export gate + FlhB (Vibrio mimicus)

  Adds FlhB, the substrate-specificity switch, to the FliPQR core. Electron microscopy, 3.2 Å.
• 7AMY
  FlhA cytoplasmic ring (nonamer)

  Nine-subunit FlhA platform under the export gate that docks substrates and chaperones. Electron microscopy, 3.75 Å.
• 3A5I
  FlhA cytoplasmic domain, Salmonella

  Salmonella FlhA-C domain for the cytoplasmic export platform. X-ray diffraction, 2.8 Å.
• 2DPY
  Export ATPase FliI

  F1-β-like ATPase of the flagellar export apparatus; evolution link to ATP synthase. X-ray diffraction, 2.4 Å.
• 3AJW
  FliJ (γ-like stalk)

  Coiled-coil export protein that resembles the ATP synthase γ stalk. X-ray diffraction, 2.1 Å.
• 1F4V
  CheY-BeF3 bound to the FliM N-terminus

  The switching signal: activated CheY (BeF3- mimics phosphate) grips the FliM N-terminal peptide. X-ray diffraction, 2.22 Å.

References

1. 1Reid et al., PNAS 2006
2. 2Chen & Berg, Biophys J 2000
3. 3Sowa et al., J Mol Biol 2003
4. 4Sowa et al., Nature 2005
5. 5Yuan & Berg, PNAS 2008
6. 6Yuan & Berg, J Mol Biol 2013
7. 7Berg, Annu Rev Biochem 2003
8. 8Cluzel et al., Science 2000
9. 9Liu et al., mBio 2020
10. 10Tu, PNAS 2008
11. 11Blair & Berg, Science 1988
12. 12Asai et al., J Mol Biol 2003
13. 13Walter et al., PNAS 2007
14. 14Beeby et al., PNAS 2016
15. 15Santiveri et al., Cell 2020
16. 16Deme et al., Nat Microbiol 2020
17. 17Hu et al., Nat Commun 2023
18. 18Nishikino et al., PNAS 2025
19. 19Johnson et al., Nat Microbiol 2024
20. 20Singh et al., Nat Microbiol 2024
21. 21Tan et al., Cell Res 2024
22. 22Tan et al., Cell 2021
23. 23Johnson et al., Nat Microbiol 2021
24. 24Johnson et al., mBio 2019
25. 25Lee et al., Nat Struct Biol 2001
26. 26Leake et al., Nature 2006
27. 27Tipping et al., mBio 2013
28. 28Lele et al., PNAS 2013
29. 29Nord et al., PNAS 2017
30. 30Abby & Rocha, PLoS Genet 2012
31. 31Imada et al., PNAS 2007
32. 32Ibuki et al., Nat Struct Mol Biol 2011
33. 33Celia et al., Nature 2016
34. 34Hennell James et al., Nat Microbiol 2021
35. 35Jarrell & Albers, Trends Microbiol 2012
36. 36Beeby et al., FEMS Microbiol Rev 2020
37. 37Park et al., ACS Nano 2017
38. 38Courbet et al., Science 2022